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Converting Peanut Protein Biomass Waste into “Double Green” Meat Substitutes Using a High-Moisture Extrusion Process: A Multiscale Method to Explore a Process for Forming a Meat-Like Fibrous Structure

Converting peanut protein biomass waste into environmentally friendly meat substitutes by a high-moisture extrusion process can help solve both resource and waste problems and be “double green”. A multiscale method combined with some emerging techniques such as atomic force microscopy-based infrared...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2019-09, Vol.67 (38), p.10713-10725
Main Authors: Zhang, Jinchuang, Liu, Li, Jiang, Yuanrong, Faisal, Shah, Wei, Linlin, Cao, Chunjie, Yan, Wenhui, Wang, Qiang
Format: Article
Language:English
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Summary:Converting peanut protein biomass waste into environmentally friendly meat substitutes by a high-moisture extrusion process can help solve both resource and waste problems and be “double green”. A multiscale method combined with some emerging techniques such as atomic force microscopy-based infrared spectroscopy and X-ray microscopy was used to make the whole extrusion process visible to show the process of forming a meat-like fibrous structure using two-dimensional and three-dimensional perspectives. The results showed that the protein molecules underwent dramatic structural changes and unfolded in the extruder barrel, which created favorable conditions for molecular rearrangement in the subsequent zones. It was confirmed that the meat-like fibrous structure started to form at the junction of the die and the cooling zone and that this structure was caused by the phase separation and rearrangement of protein molecules in the cooling zone. Moreover, the interactions between hydrogen bonds and disulfide bonds formed in the cooling zone maintained the meat-like fibrous structure with an α-helix > β-sheet > β-turn > random coil. Of the two main peanut proteins, arachin played a greater role in forming the fibrous structure than conarachin, especially those subunits of arachin with a molecular weight of 42, 39, and 22 kDa.
ISSN:0021-8561
1520-5118
DOI:10.1021/acs.jafc.9b02711